Header list of 1s1n.pdb file
Complete list - n 24 2 Bytes
HEADER CELL ADHESION 07-JAN-04 1S1N TITLE SH3 DOMAIN OF HUMAN NEPHROCYSTIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEPHROCYSTIN 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SH3 DOMAIN; COMPND 5 SYNONYM: JUVENILE NEPHRONOPHTHISIS 1 PROTEIN; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: NPHP1, NPH1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-2 KEYWDS BETA BARREL, CELL ADHESION EXPDTA SOLUTION NMR NUMMDL 17 AUTHOR A.LE MAIRE,T.WEBER,S.SAUNIER,C.ANTIGNAC,A.DUCRUIX,F.DARDEL REVDAT 4 24-JAN-18 1S1N 1 JRNL REMARK REVDAT 3 24-FEB-09 1S1N 1 VERSN REVDAT 2 19-APR-05 1S1N 1 JRNL REVDAT 1 18-JAN-05 1S1N 0 JRNL AUTH A.LE MAIRE,T.WEBER,S.SAUNIER,I.BROUTIN,C.ANTIGNAC,A.DUCRUIX, JRNL AUTH 2 F.DARDEL JRNL TITL SOLUTION NMR STRUCTURE OF THE SH3 DOMAIN OF HUMAN JRNL TITL 2 NEPHROCYSTIN AND ANALYSIS OF A MUTATION-CAUSING JUVENILE JRNL TITL 3 NEPHRONOPHTHISIS. JRNL REF PROTEINS V. 59 347 2005 JRNL REFN ISSN 0887-3585 JRNL PMID 15723349 JRNL DOI 10.1002/PROT.20344 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.SAUNIER,J.CALADO,R.HEILIG,F.SILBERMANN,F.BENESSY,G.MORIN, REMARK 1 AUTH 2 M.KONRAD,M.BROYER,M.C.GUBLER,J.WEISSENBACH REMARK 1 TITL A NOVEL GENE THAT ENCODES A PROTEIN WITH A PUTATIVE SRC REMARK 1 TITL 2 HOMOLOGY 3 DOMAIN IS A CANDIDATE GENE FOR FAMILIAL JUVENILE REMARK 1 TITL 3 NEPHRONOPHTHISIS REMARK 1 REF HUM.MOL.GENET. V. 6 21317 1997 REMARK 1 REFN ISSN 0964-6906 REMARK 1 DOI 10.1093/HMG/6.13.2317 REMARK 1 REFERENCE 2 REMARK 1 AUTH F.HILDEBRANDT,E.OTTO,C.RENSIG,H.G.NOTHWANG,M.VOLLMER, REMARK 1 AUTH 2 J.ADOLPHS,H.HANUSH,M.BRANDIS REMARK 1 TITL A NOVEL GENE ENCODING AN SH3 DOMAIN PROTEIN IS MUTATED IN REMARK 1 TITL 2 NEPHRONOPHTHISIS TYPE 1 REMARK 1 REF NAT.GENET. V. 17 149 1997 REMARK 1 REFN ISSN 1061-4036 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DIANA 2.8, X-PLOR 3.89 REMARK 3 AUTHORS : GUENTERT (DIANA), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 623 RESTRAINTS. REMARK 3 540 ARE NOE-DERIVED RESTRAINTS : 110 INTRARESIDUE, 121 SEQUENTIAL, REMARK 3 37 MEDIUM-RANGE AND 272 LONG-RANGE. REMARK 3 30 DISTANCE RESTRAINTS FROM HYDROGEN BONDS. REMARK 3 53 DIHEDRAL ANGLE RESTRAINTS. REMARK 4 REMARK 4 1S1N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-04. REMARK 100 THE DEPOSITION ID IS D_1000021253. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 20 MM K-PHOSPHATE REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.5 MM SH3 DOMAIN U-15N,13C; REMARK 210 20MM PHOSPHATE BUFFER K, PH6.5 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; HNHA; HNHB; 2D REMARK 210 NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : DISTANCE GEOMETRY FOLLWED BY REMARK 210 RESTRAINED SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-17 REMARK 465 RES C SSSEQI REMARK 465 GLY A 145 REMARK 465 SER A 146 REMARK 465 GLU A 147 REMARK 465 SER A 148 REMARK 465 HIS A 149 REMARK 465 LYS A 150 REMARK 465 TRP A 151 REMARK 465 SER A 152 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 1 TRP A 189 CG - CD1 - NE1 ANGL. DEV. = -6.9 DEGREES REMARK 500 1 TRP A 189 CD1 - NE1 - CE2 ANGL. DEV. = 7.7 DEGREES REMARK 500 1 TRP A 189 NE1 - CE2 - CZ2 ANGL. DEV. = 7.6 DEGREES REMARK 500 1 TRP A 190 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES REMARK 500 1 TRP A 190 CD1 - NE1 - CE2 ANGL. DEV. = 8.5 DEGREES REMARK 500 2 TRP A 189 CG - CD1 - NE1 ANGL. DEV. = -7.4 DEGREES REMARK 500 2 TRP A 189 CD1 - NE1 - CE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 2 TRP A 189 NE1 - CE2 - CZ2 ANGL. DEV. = 8.6 DEGREES REMARK 500 2 TRP A 190 CG - CD1 - NE1 ANGL. DEV. = -7.1 DEGREES REMARK 500 2 TRP A 190 CD1 - NE1 - CE2 ANGL. DEV. = 8.7 DEGREES REMARK 500 2 TRP A 190 NE1 - CE2 - CZ2 ANGL. DEV. = 6.9 DEGREES REMARK 500 3 TRP A 189 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES REMARK 500 3 TRP A 189 CD1 - NE1 - CE2 ANGL. DEV. = 7.8 DEGREES REMARK 500 3 TRP A 189 NE1 - CE2 - CZ2 ANGL. DEV. = 8.4 DEGREES REMARK 500 3 TRP A 190 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES REMARK 500 3 TRP A 190 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES REMARK 500 4 TYR A 157 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES REMARK 500 4 TYR A 157 CB - CG - CD1 ANGL. DEV. = 3.9 DEGREES REMARK 500 4 ILE A 178 CA - CB - CG1 ANGL. DEV. = -13.6 DEGREES REMARK 500 4 TRP A 189 CG - CD1 - NE1 ANGL. DEV. = -6.8 DEGREES REMARK 500 4 TRP A 189 CD1 - NE1 - CE2 ANGL. DEV. = 7.8 DEGREES REMARK 500 4 TRP A 189 NE1 - CE2 - CZ2 ANGL. DEV. = 7.6 DEGREES REMARK 500 4 TRP A 190 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES REMARK 500 4 TRP A 190 CD1 - NE1 - CE2 ANGL. DEV. = 8.6 DEGREES REMARK 500 4 TRP A 190 NE1 - CE2 - CZ2 ANGL. DEV. = 7.0 DEGREES REMARK 500 5 TRP A 189 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES REMARK 500 5 TRP A 189 CD1 - NE1 - CE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 5 TRP A 189 NE1 - CE2 - CZ2 ANGL. DEV. = 8.1 DEGREES REMARK 500 5 TRP A 190 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES REMARK 500 5 TRP A 190 CD1 - NE1 - CE2 ANGL. DEV. = 8.5 DEGREES REMARK 500 5 TRP A 190 NE1 - CE2 - CZ2 ANGL. DEV. = 7.9 DEGREES REMARK 500 6 TRP A 189 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES REMARK 500 6 TRP A 189 CD1 - NE1 - CE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 6 TRP A 189 NE1 - CE2 - CZ2 ANGL. DEV. = 8.4 DEGREES REMARK 500 6 TRP A 190 CG - CD1 - NE1 ANGL. DEV. = -7.1 DEGREES REMARK 500 6 TRP A 190 CD1 - NE1 - CE2 ANGL. DEV. = 8.7 DEGREES REMARK 500 7 TRP A 189 CG - CD1 - NE1 ANGL. DEV. = -6.9 DEGREES REMARK 500 7 TRP A 189 CD1 - NE1 - CE2 ANGL. DEV. = 7.7 DEGREES REMARK 500 7 TRP A 189 NE1 - CE2 - CZ2 ANGL. DEV. = 7.4 DEGREES REMARK 500 7 TRP A 190 CG - CD1 - NE1 ANGL. DEV. = -7.1 DEGREES REMARK 500 7 TRP A 190 CD1 - NE1 - CE2 ANGL. DEV. = 8.7 DEGREES REMARK 500 8 TRP A 189 CG - CD1 - NE1 ANGL. DEV. = -7.1 DEGREES REMARK 500 8 TRP A 189 CD1 - NE1 - CE2 ANGL. DEV. = 7.7 DEGREES REMARK 500 8 TRP A 189 NE1 - CE2 - CZ2 ANGL. DEV. = 8.2 DEGREES REMARK 500 8 TRP A 190 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES REMARK 500 8 TRP A 190 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES REMARK 500 9 TRP A 189 CG - CD1 - NE1 ANGL. DEV. = -7.1 DEGREES REMARK 500 9 TRP A 189 CD1 - NE1 - CE2 ANGL. DEV. = 7.7 DEGREES REMARK 500 9 TRP A 189 NE1 - CE2 - CZ2 ANGL. DEV. = 8.1 DEGREES REMARK 500 9 TRP A 190 CG - CD1 - NE1 ANGL. DEV. = -7.4 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 105 ANGLE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 1 LYS A 175 77.95 -23.90 REMARK 500 1 GLU A 183 153.18 130.56 REMARK 500 1 LYS A 185 78.37 -9.79 REMARK 500 1 ASP A 194 -163.23 -122.45 REMARK 500 1 ALA A 195 40.86 -103.36 REMARK 500 1 THR A 205 -53.67 -23.44 REMARK 500 1 SER A 211 73.55 -110.75 REMARK 500 2 ASP A 162 78.06 -104.90 REMARK 500 2 VAL A 168 45.42 -96.83 REMARK 500 2 LYS A 174 62.98 -118.51 REMARK 500 2 LYS A 175 76.83 37.05 REMARK 500 2 GLU A 183 151.26 131.08 REMARK 500 2 LYS A 185 80.67 -12.43 REMARK 500 2 ASP A 194 -159.12 -119.67 REMARK 500 2 THR A 205 -46.03 -23.21 REMARK 500 2 TYR A 206 51.78 -106.12 REMARK 500 2 SER A 211 52.00 -119.45 REMARK 500 3 VAL A 168 40.22 -94.37 REMARK 500 3 LYS A 175 76.25 -22.25 REMARK 500 3 GLU A 183 155.80 140.10 REMARK 500 3 LYS A 185 86.70 -15.52 REMARK 500 3 ASP A 194 -163.76 -122.75 REMARK 500 3 ALA A 195 40.93 -98.87 REMARK 500 3 THR A 205 -52.73 -23.55 REMARK 500 3 SER A 211 63.05 -100.72 REMARK 500 4 LYS A 175 154.37 -39.02 REMARK 500 4 GLU A 183 150.59 136.14 REMARK 500 4 LYS A 185 77.40 -10.70 REMARK 500 4 ASP A 194 -165.91 -121.19 REMARK 500 4 ALA A 195 40.44 -106.15 REMARK 500 4 THR A 205 -50.97 -28.87 REMARK 500 4 TYR A 210 -99.27 -116.70 REMARK 500 4 SER A 211 -52.22 -125.69 REMARK 500 5 LYS A 175 80.66 -35.07 REMARK 500 5 GLU A 183 141.53 125.35 REMARK 500 5 LYS A 185 75.75 -14.37 REMARK 500 5 ASP A 194 -162.63 -126.35 REMARK 500 5 ALA A 195 40.85 -98.96 REMARK 500 5 THR A 205 -48.55 -18.37 REMARK 500 6 ASP A 162 76.14 -106.06 REMARK 500 6 LYS A 174 62.21 -114.99 REMARK 500 6 LYS A 175 74.12 41.02 REMARK 500 6 GLU A 183 154.13 142.32 REMARK 500 6 LYS A 185 81.18 -7.27 REMARK 500 6 ASP A 194 -162.78 -120.12 REMARK 500 6 ALA A 195 39.44 -99.54 REMARK 500 6 THR A 205 -51.31 -25.56 REMARK 500 6 TYR A 206 50.43 -113.88 REMARK 500 7 VAL A 168 47.21 -95.45 REMARK 500 7 THR A 172 -69.24 -120.88 REMARK 500 REMARK 500 THIS ENTRY HAS 127 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 204 0.22 SIDE CHAIN REMARK 500 2 ARG A 204 0.27 SIDE CHAIN REMARK 500 3 ARG A 204 0.16 SIDE CHAIN REMARK 500 4 ARG A 204 0.30 SIDE CHAIN REMARK 500 5 ARG A 204 0.32 SIDE CHAIN REMARK 500 6 ARG A 204 0.16 SIDE CHAIN REMARK 500 7 ARG A 204 0.31 SIDE CHAIN REMARK 500 8 ARG A 204 0.12 SIDE CHAIN REMARK 500 9 ARG A 204 0.32 SIDE CHAIN REMARK 500 10 ARG A 204 0.29 SIDE CHAIN REMARK 500 11 ARG A 204 0.31 SIDE CHAIN REMARK 500 12 ARG A 204 0.28 SIDE CHAIN REMARK 500 13 ARG A 204 0.28 SIDE CHAIN REMARK 500 14 ARG A 204 0.32 SIDE CHAIN REMARK 500 15 ARG A 204 0.32 SIDE CHAIN REMARK 500 16 ARG A 204 0.31 SIDE CHAIN REMARK 500 17 ARG A 204 0.16 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1S1N A 147 212 UNP O15259 NPHP1_HUMAN 147 212 SEQADV 1S1N GLY A 145 UNP O15259 CLONING ARTIFACT SEQADV 1S1N SER A 146 UNP O15259 CLONING ARTIFACT SEQRES 1 A 68 GLY SER GLU SER HIS LYS TRP SER THR GLY GLU GLU TYR SEQRES 2 A 68 ILE ALA VAL GLY ASP PHE THR ALA GLN GLN VAL GLY ASP SEQRES 3 A 68 LEU THR PHE LYS LYS GLY GLU ILE LEU LEU VAL ILE GLU SEQRES 4 A 68 LYS LYS PRO ASP GLY TRP TRP ILE ALA LYS ASP ALA LYS SEQRES 5 A 68 GLY ASN GLU GLY LEU VAL PRO ARG THR TYR LEU GLU PRO SEQRES 6 A 68 TYR SER GLU SHEET 1 A 5 GLU A 199 PRO A 203 0 SHEET 2 A 5 TRP A 189 LYS A 193 -1 N TRP A 190 O VAL A 202 SHEET 3 A 5 GLU A 177 VAL A 181 -1 N LEU A 180 O LYS A 193 SHEET 4 A 5 GLU A 155 ALA A 159 -1 N TYR A 157 O LEU A 179 SHEET 5 A 5 LEU A 207 PRO A 209 -1 O GLU A 208 N ILE A 158 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 MODEL 1
Complete list - n 24 2 Bytes